title: Conformational change of Sos-derived proline-rich peptide upon binding Grb2 N-terminal SH3 domain probed by NMR.
abstract: Growth factor receptor-bound protein 2 (Grb2) is a small adapter protein composed of a single SH2 domain flanked by two SH3 domains. The N-terminal SH3 (nSH3) domain of Grb2 binds a proline-rich region present in the guanine nucleotide releasing factor, son of sevenless (Sos). Using NMR relaxation dispersion and chemical shift analysis methods, we investigated the conformational change of the Sos-derived proline-rich peptide during the transition between the free and Grb2 nSH3-bound states. The chemical shift analysis revealed that the peptide does not present a fully random conformation but has a relatively rigid structure. The relaxation dispersion analysis detected conformational exchange of several residues of the peptide upon binding to Grb2 nSH3.
authors.affiliation: Department of Structural Biology, Faculty of Advanced Life Science, Hokkaido University, Kita 21 Nishi 11, Kita-ku, Sapporo 001-0021, Japan.
authors.forename: Kenji
authors.initials: K
authors.lastname: Ogura
authors.forename: Hideyasu
authors.initials: H
authors.lastname: Okamura
mesh_terms: D051380:GRB2 Adaptor Protein / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008279:Magnetic Resonance Imaging / Q000379:methods*; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism; D055232:Proline-Rich Protein Domains; D011487:Protein Conformation; D020664:Son of Sevenless Proteins / Q000737:chemistry* / Q000378:metabolism; D018909:src Homology Domains
chemical_list: D051380:GRB2 Adaptor Protein; D010446:Peptide Fragments; D020664:Son of Sevenless Proteins